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FEBS Lett. 2002 Jun 5;520(1-3):107-10.

Cdc48 can distinguish between native and non-native proteins in the absence of cofactors.

Author information

1
ZMBH, Center for Molecular Biology, Heidelberg University, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany. s.thoms@zmbh.uni-heidelberg.de

Abstract

The ATPase Cdc48 is required for membrane fusion and protein degradation. Recently it has been suggested that Cdc48 in a complex with Ufd1 and Npl4 acts as an ubiquitin-dependent chaperone. Here it is shown that recombinant Cdc48 alone can distinguish between the native and the non-native conformation of model substrates. First, Cdc48 prevents luciferase from aggregating following a heat shock. Second, it inhibits the aggregation of rhodanese upon dilution. Third, Cdc48 binds specifically to heat-denatured luciferase. These chaperone-like functions seem to be independent of ATPase activity. Furthermore, Cdc48 can act as a co-chaperone in the Hsc70-Hsp40 chaperone system. These results show that Cdc48 possesses chaperone-like activities and can functionally interact with Hsc70. Cdc48's ability to recognise denatured proteins can also be a source of unspecific binding in biochemical interaction experiments.

PMID:
12044880
DOI:
10.1016/s0014-5793(02)02777-1
[Indexed for MEDLINE]
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